Fraser obtained a BSc in Chemistry from the University of Sheffield in 1987 and a Dr. rer. nat. from the Department of Chemistry at the Free University of Berlin (Germany) in 1993. He pursued post-doctoral research at the Technical University Berlin (Germany) (1993-1995), the Commissariat de l’Energie Atomique, Saclay, France (1995-1998) and the Johann Wolfgang Goethe-University Frankfurt (Germany) (1998-2006).

Fraser is currently a Reader in the School of Chemistry at the University of East Anglia, Norwich where he joined the faculty in 2007. To coincide with his appointment Fraser has won a Royal Society Wolfson Research Merit Award. He leads biological EPR research in the Henry Welcome Laboratory.

His present research aims to elucidate structure / function / dynamics relationships in biomacromolecules and macromolecular complexes. Particular emphasis being on the application, and expansion, of electron paramagnetic resonance methods to study membrane proteins.

Membrane and metalloproteins including photosynthetic and respiratory proteins

Structure/function/dynamics relationships in biomacromolecules

Electron transfer and (ABC-)transporter proteins

Current Methodologies/Techniques Used

All modern advanced EPR spectroscopies

MO-calculations (DFT)

Freeze-quenching

Spin labelling

Areas for Potential Collaboration:Anywhere where structural or structure/functional (including dynamic) information of a biomacromolecule is of importance. While endogenous spin probes (transition metal ion cofactors, organic cofactors or protein based radicals) are the probes of choice for the methods we apply, the use of exogenous spin probes (nitroxide spin labels and transition metal ions) also allows us to address inherently diamagnetic proteins and protein complexes, permitting access to similar information in these cases.

Current Research Projects: My interests lie in the application and development of modern paramagnetic resonance spectroscopic techniques to characterise and correlate the structure and function of biomacromolecules. We apply advanced EPR techniques to study both local and global interactions of endogenous as well as exogneous spin probes providing very detailed structural information, which can be considered complementary to crystallographic and other structural techniques. In principle we are able to work with isolated proteins, protein ensembles, enriched membrane fragments, proteins reconstituted in proteoliposomes as well as in whole cells. Selected current active collaborations outside UEA include work on transporter proteins (p-Glycoprotein (Oxford), ATP-transporters (MRC Cambridge), respiratory proteins (complexes I, II, III and IV (Philadelphia, San Francisco, Freiburg, Newcastle and Frankfurt)), Colicins (York, Nottingham) and photosynthetic proteins (bioenergy systems (Tempe, Columbia)).